Reactant A decomposes to products B and C in the presence of an enzyme in a well-stirred batch reactor. The kinetic rate expression is given by
\[ -r_A = \frac{0.01 C_A}{0.05 + C_A} \, \text{(mol L}^{-1} \text{min}^{-1}) \] If the initial concentration of A is 0.02 mol L\(^{-1}\), the time taken to achieve 50% conversion of A is \(\underline{\hspace{1cm}}\) min (rounded to 2 decimal places).
In an enzymatic reaction, an inhibitor (I) competes with the substrate (S) to bind with the enzyme (E), thereby reducing the rate of product (P) formation. The competitive inhibition follows the reaction mechanism shown below. Let [S] and [I] be the concentration of S and I, respectively, and $r_s$ be the rate of consumption of S. Assuming pseudo-steady state, the correct plot of $\frac{1}{-r_s}$ vs $\frac{1}{[S]}$ is

